STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
prfBPeptide chain release factor 2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. (319 aa)    
Predicted Functional Partners:
rplM
LSU ribosomal protein L13p; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
   0.976
rplU
LSU ribosomal protein L21p; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
   
   0.972
rpsG
SSU ribosomal protein S7p; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
 
 
 0.968
rpmA
LSU ribosomal protein L27p; Belongs to the bacterial ribosomal protein bL27 family.
 
 
 0.967
rpsP
SSU ribosomal protein S16p; Belongs to the bacterial ribosomal protein bS16 family.
 
 
 0.966
rplT
LSU ribosomal protein L20p; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
  
 
 0.966
rpsL
SSU ribosomal protein S12p; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
 
 
 0.963
rpsR
SSU ribosomal protein S18p; Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit; Belongs to the bacterial ribosomal protein bS18 family.
 
 
 0.962
rplF
LSU ribosomal protein L6p; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
  
   0.961
rplB
LSU ribosomal protein L2p; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
   
   0.959
Your Current Organism:
Archangium gephyra
NCBI taxonomy Id: 48
Other names: A. gephyra, ATCC 25201, Chondrococcus cerebriformis, Chondromyces serpens, DSM 2261, Myxococcus cerebriformis
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.